Influenza A H7N9 (A/Anhui/1-BALF_RG6/2013) Nucleoprotein/NP Protein (His) is expressed in Baculovirus insect cells with His tag. The predicted molecular weight is 57.8 kDa and the accession number is A0A024E372.

Influenza A H1N1 (A/Brevig Mission/1/1918) Nucleoprotein/NP Protein (His) is expressed in Baculovirus insect cells with His tag. The predicted molecular weight is 57.7 kDa and the accession number is Q5UEW0.1.

Neuropilin-1 Protein, Mouse, Recombinant (His) is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 95.12 kDa and the accession number is P97333.

SARS-COV-2 BQ.1/BQ.1.1 (Omicron) Nucleoprotein/NP Protein (His) is expressed in E. coli expression system with His tag. The predicted molecular weight is 46.36 kDa and the accession number is YP_009724397.2.

Neuropilin-1 Protein, Mouse, Recombinant (mFc) is expressed in HEK293 mammalian cells with mFc tag. The predicted molecular weight is 120 kDa and the accession number is P97333.

Encapsidates the negative strand viral RNA, protecting it from nucleases. The encapsidated genomic RNA is termed the ribonucleoprotein (RNP) and serves as template for transcription and replication. The RNP needs to be localized in the host nucleus to start an infectious cycle, but is too large to diffuse through the nuclear pore complex. NP comprises at least 2 nuclear localization signals that are responsible for the active RNP import into the nucleus through cellular importin alpha/beta pathway. Later in the infection, nclear export of RNPs are mediated through viral proteins NEP interacting with M1 which binds nucleoproteins. It is possible that nucleoprotein binds directly host exportin-1/XPO1 and plays an active role in RNPs nuclear export. M1 interaction with RNP seems to hide nucleoprotein's nuclear localization signals. Soon after a virion infects a new cell, M1 dissociates from the RNP under acidification of the virion driven by M2 protein. Dissociation of M1 from RNP unmasks nucleoprotein's nuclear localization signals, targeting the RNP to the nucleus.

Encapsidates the negative strand viral RNA, protecting it from nucleases. The encapsidated genomic RNA is termed the ribonucleoprotein (RNP) and serves as template for transcription and replication. The RNP needs to be localized in the host nucleus to start an infectious cycle, but is too large to diffuse through the nuclear pore complex. NP comprises at least 2 nuclear localization signals that are responsible for the active RNP import into the nucleus through cellular importin alpha/beta pathway. Later in the infection, nclear export of RNPs are mediated through viral proteins NEP interacting with M1 which binds nucleoproteins. It is possible that nucleoprotein binds directly host exportin-1/XPO1 and plays an active role in RNPs nuclear export. M1 interaction with RNP seems to hide nucleoprotein's nuclear localization signals. Soon after a virion infects a new cell, M1 dissociates from the RNP under acidification of the virion driven by M2 protein. Dissociation of M1 from RNP unmasks nucleoprotein's nuclear localization signals, targeting the RNP to the nucleus.

Influenza A H3N2 (A/Hong Kong/1/1968) Nucleoprotein/NP Protein (His) is expressed in Baculovirus insect cells with His tag. The predicted molecular weight is 57.5 kDa and the accession number is P22435.2.

Encapsidates the genome in a ratio of 1 N per 6 ribonucleotides, protecting it from nucleases. The nucleocapsid (NC) has a helical structure. The encapsidated genomic RNA is termed the NC and serves as template for transcription and replication. During replication, encapsidation by N is coupled to RNA synthesis and all replicative products are resistant to nucleases. Human parainfluenza 1 virus (HPIV-1) Nucleoprotein/NP Protein (His) is expressed in E. coli expression system with N-10xHis tag. The predicted molecular weight is 63.6 kDa and the accession number is P24304.

Neuropilin-1 Protein, Human, Recombinant (His) is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 71.33 kDa and the accession number is NP_001019799.2.

Neuropilin-1 Protein, Human, Recombinant (Avi & His), Biotinylated is expressed in HEK293 mammalian cells with His and Avi tag. The predicted molecular weight is 73.1 kDa and the accession number is O14786-2.

Encapsidates the negative strand viral RNA, protecting it from nucleases. The encapsidated genomic RNA is termed the ribonucleoprotein (RNP) and serves as template for transcription and replication. The RNP needs to be localized in the host nucleus to start an infectious cycle, but is too large to diffuse through the nuclear pore complex. NP comprises at least 2 nuclear localization signals that are responsible for the active RNP import into the nucleus through cellular importin alpha/beta pathway. Later in the infection, nclear export of RNPs are mediated through viral proteins NEP interacting with M1 which binds nucleoproteins. It is possible that nucleoprotein binds directly host exportin-1/XPO1 and plays an active role in RNPs nuclear export. M1 interaction with RNP seems to hide nucleoprotein's nuclear localization signals. Soon after a virion infects a new cell, M1 dissociates from the RNP under acidification of the virion driven by M2 protein. Dissociation of M1 from RNP unmasks nucleoprotein's nuclear localization signals, targeting the RNP to the nucleus.

Neuronal Pentraxin (NPTX1, NP1) is a secreted glycoprotein within the Pentraxin family. NPTX1 is co‑expressed and forms heteromultimers with the related secreted protein, NPTX2/NARP, NPTXR (Neuronal Pentraxin Receptor) at excitatory synapses. Mature human NPTX1 shares 97% aa sequence identity with mouse, and rat NPTX1. It is produced by hippocampal, cerebral and cerebellar neurons, retinal ganglia and the inner nuclear layer of the retina. It is enriched on presynaptic axonal membranes where it forms complexes with NPTXR. It may be involved in mediating uptake of synaptic material during synapse remodeling or in mediating the synaptic clustering of AMPA glutamate receptors at a subset of excitatory synapses.

Neuropilin-1 Protein, Human, Recombinant (isoform b, His) is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 71.3 kDa and the accession number is O14786-2.

Encapsidates the negative strand viral RNA, protecting it from nucleases. The encapsidated genomic RNA is termed the ribonucleoprotein (RNP) and serves as template for transcription and replication. The RNP needs to be localized in the host nucleus to start an infectious cycle, but is too large to diffuse through the nuclear pore complex. NP comprises at least 2 nuclear localization signals that are responsible for the active RNP import into the nucleus through cellular importin alpha/beta pathway. Later in the infection, nclear export of RNPs are mediated through viral proteins NEP interacting with M1 which binds nucleoproteins. It is possible that nucleoprotein binds directly host exportin-1/XPO1 and plays an active role in RNPs nuclear export. M1 interaction with RNP seems to hide nucleoprotein's nuclear localization signals. Soon after a virion infects a new cell, M1 dissociates from the RNP under acidification of the virion driven by M2 protein. Dissociation of M1 from RNP unmasks nucleoprotein's nuclear localization signals, targeting the RNP to the nucleus.

Neuropilin-1 Protein, Human, Recombinant (V179A, hFc) is expressed in HEK293 mammalian cells with hFc tag. The predicted molecular weight is 96.5 kDa and the accession number is O14786-2.

Neuropilin-1 Protein, Human, Recombinant (aa 1-64, N150Q, His) is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 71.31 kDa and the accession number is NP_001019799.2.

Encapsidates the negative strand viral RNA, protecting it from nucleases. The encapsidated genomic RNA is termed the ribonucleoprotein (RNP) and serves as template for transcription and replication. The RNP needs to be localized in the host nucleus to start an infectious cycle, but is too large to diffuse through the nuclear pore complex. NP comprises at least 2 nuclear localization signals that are responsible for the active RNP import into the nucleus through cellular importin alpha/beta pathway. Later in the infection, nclear export of RNPs are mediated through viral proteins NEP interacting with M1 which binds nucleoproteins. It is possible that nucleoprotein binds directly host exportin-1/XPO1 and plays an active role in RNPs nuclear export. M1 interaction with RNP seems to hide nucleoprotein's nuclear localization signals. Soon after a virion infects a new cell, M1 dissociates from the RNP under acidification of the virion driven by M2 protein. Dissociation of M1 from RNP unmasks nucleoprotein's nuclear localization signals, targeting the RNP to the nucleus.

Influenza A H2N2 (A/Ann Arbor/6/1960) Nucleoprotein/NP Protein (His) is expressed in Baculovirus insect cells with His tag. The predicted molecular weight is 57 kDa and the accession number is P21433-1.

Encapsidates the negative strand viral RNA, protecting it from nucleases. The encapsidated genomic RNA is termed the ribonucleoprotein (RNP) and serves as template for transcription and replication. The RNP needs to be localized in the host nucleus to start an infectious cycle, but is too large to diffuse through the nuclear pore complex. NP comprises at least 2 nuclear localization signals that are responsible for the active RNP import into the nucleus through cellular importin alpha/beta pathway. Later in the infection, nclear export of RNPs are mediated through viral proteins NEP interacting with M1 which binds nucleoproteins. It is possible that nucleoprotein binds directly host exportin-1/XPO1 and plays an active role in RNPs nuclear export. M1 interaction with RNP seems to hide nucleoprotein's nuclear localization signals. Soon after a virion infects a new cell, M1 dissociates from the RNP under acidification of the virion driven by M2 protein. Dissociation of M1 from RNP unmasks nucleoprotein's nuclear localization signals, targeting the RNP to the nucleus.